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Purification and properties of an alcohol dehydrogenase (HUADHII) from Hanseniaspora uvarum K 5
Author(s) -
Venturin C.,
Zulaika J.,
Boze H.,
Moulin G.,
Galzy P.
Publication year - 1995
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1995.tb03127.x
Subject(s) - kluyveromyces lactis , alcohol dehydrogenase , enzyme , biochemistry , chemistry , stereochemistry , alcohol , kluyveromyces , saccharomyces cerevisiae , ethanol , yeast , protonation , organic chemistry , ion
An alcohol dehydrogenase HUADHII was purified 43.2‐fold from Hanseniaspora uvarum K 5 . The enzyme was trimeric with subunits of mol. wt 42 kDa. The N ‐terminal amino acid sequence of HUADHII has between 45 and 75% identity with part of the sequence of isoenzymes related to group I from Saccharomyces cerevisiae and Kluyveromyces lactis. C2–C4 alcohols and aldehydes were the preferred substrates. The presence of an’α’double bond increased the enzyme activity both for alcohols and aldehydes. It was significantly inhibited by metal‐binding agents and thiol reagents. Kinetic studies suggested that HUADHII catalyses the oxidation of ethanol by a random sequential mechanism. It appears that HUADHII, a cytoplasmic fermentative enzyme, is structurally and functionally similar to members of the group I alcohol dehydrogenases.